HSP90_THEPA
ID HSP90_THEPA Reviewed; 721 AA.
AC P24724; Q4N5P6;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Heat shock protein 90;
DE Short=HSP90;
GN OrderedLocusNames=TP02_0244;
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gerhards J., Morzarin S.P., Musoke A.J., Lipp J., Williams R.O.;
RT "Sequence and expression of a 90 kilodalton heat-shock protein.";
RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga;
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(2005).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity. This cycle
CC probably induces conformational changes in the client proteins, thereby
CC causing their activation. Interacts dynamically with various co-
CC chaperones that modulate its substrate recognition, ATPase cycle and
CC chaperone function (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; M57386; AAA30132.1; -; mRNA.
DR EMBL; AAGK01000002; EAN32527.1; -; Genomic_DNA.
DR RefSeq; XP_764810.1; XM_759717.1.
DR AlphaFoldDB; P24724; -.
DR SMR; P24724; -.
DR STRING; 5875.XP_764810.1; -.
DR PRIDE; P24724; -.
DR EnsemblProtists; EAN32527; EAN32527; TP02_0244.
DR GeneID; 3501902; -.
DR KEGG; tpv:TP02_0244; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_02g00244; -.
DR eggNOG; KOG0019; Eukaryota.
DR InParanoid; P24724; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000001949; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..721
FT /note="Heat shock protein 90"
FT /id="PRO_0000062943"
FT REGION 219..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 717..721
FT /note="TPR repeat-binding"
FT COMPBIAS 235..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 508
FT /note="A -> S (in Ref. 1; AAA30132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 83668 MW; A745C2B3B50ED924 CRC64;
MTSKDETPDQ EVYAFNADIS QLLSLIINAF YSNKEIFLRE LISNASDALE KIRYEAIKDP
KQIEDQPDYY IRLYADKNNN TLTIEDSGIG MTKADLVNNL GTIAKSGTRA FMEALQAGSD
MSMIGQFGVG FYSAYLVADK VTVVSKNNAD DQYVWESTAS GHFTVKKDDS HEPLKRGTRL
ILHLKEDQTE YLEERRLKEL VKKHSEFISF PISLSVEKTQ ETEVTDDEAE LDEDKKPEEE
KPKDDKVEDV TDEKVTDVTD EEEKKEEKKK KKRKVTNVTR EWEMLNKQKP IWMRLPSEVT
NEEYAAFYKN LTNDWEDHLA VKHFSVEGQL EFKALLFVPR RAPFDMFESR KKKNNIKLYV
RRVFIMDDCE ELIPEWLSFV KGVVDSEDLP LNISRETLQQ NKILKVIRKN LVKKCLELFN
ELTEKKEDFK KFYEQFSKNL KLGIHEDNAN RSKIAELLRF ETTKSGDELV SLKEYVDRMK
SDQKYVYYIT GESKQSVASS PFLETLRARD YEVLYMTDPI DEYAVQQIKE FEGKKLKCCT
KEGLDLDEGE DEKKSFEALK EEMEPLCKHI KEVLHDKVEK VVCGTRFTDS PCALVTSEFG
WSANMERIMK AQALRDSSIT SYMLSKKIME INPRHSIMKE LKTRAANDKT DKTVKDLVWL
LYDTALLTSG FNLDEPTQFG NRIYRMIKLG LSLDDEEHVE EDSSMPPLDE PVVDSKMEEV
D
